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- W19252034 abstract "Protein refolding was simulated by minimizing the hydrophobic (as well as van der Waals) energies between side chains, which were approximated as single spheres. Secondary structures were fixed in advance, allowing only dihedral angles in the loop regions to vary. Energy minimization was performed separately for each loop region by merging minimizing regions step by step, so that the resulting structure depended on the initial choice of the minimization ordering. The method was applied to three α-proteins ; cytochrome b562, the amino-terminal domain of phage 434 repressor and murine interferon- β . Among the minimized structures with different refolding orders, native-like structures were found for cytochrome b562 and the amino-terminal domain of phage 434 repressor. For these proteins the best structures showed 3.96 a and 4.99 a root mean squares (rms-S) deviations, respectively, when superimposed on the X-ray structure." @default.
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- W19252034 date "1993-01-01" @default.
- W19252034 modified "2023-09-23" @default.
- W19252034 title "Prediction of tertiary structure of protein by folding simulation using hydrophobic interaction" @default.
- W19252034 cites W1992983202 @default.
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- W19252034 doi "https://doi.org/10.1016/b978-0-444-89778-7.50090-6" @default.
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